The esterase profile of a lipase from Candida cylindracea.
A commercial preparation of a lipase produced by Candida cylindracea catalysed the hydrolysis of both long- and short-chain esters of p-nitrophenol. Six major bands of hydrolytic activity to alpha-naphthyl acetate were detected on polyacrylamide gel electrophoresis and two on isoelectric focusing. The esterase activity fractionated into two major peaks of activity on ion-exchange chromatography and into several peaks of activity on hydrophobic interaction chromatography. These esterase activities showed different substrate specificities to p-nitrophenyl esters, tributyrin and cetyl palmitate.
Brahimi-Horn
M C
MC
Commonwealth Scientific and Industrial Research Organization, Division of Wool Technology, Parkvill Laboratory, Australia.
Guglielmino
M L
ML
Elling
L
L
Sparrow
L G
LG
D002175:Candida / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004950:Esterases / Q000378:metabolism*; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008049:Lipase / Q000378:metabolism*; D013379:Substrate Specificity
D004950:Esterases; D008049:Lipase